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  • Amino Acid Sequence  (50)
  • American Association for the Advancement of Science (AAAS)  (50)
  • Elsevier
  • American Institute of Physics (AIP)
  • 1985-1989  (50)
  • 1985  (50)
Sammlung
Verlag/Herausgeber
  • American Association for the Advancement of Science (AAAS)  (50)
  • Elsevier
  • American Institute of Physics (AIP)
Erscheinungszeitraum
  • 1985-1989  (50)
Jahr
  • 1
    Publikationsdatum: 1985-11-15
    Beschreibung: A newly identified protein from HTLV-III/LAV, the virus implicated as the etiologic agent of the acquired immune deficiency syndrome, was studied. This protein, which has a molecular weight of 27,000 (p27), was shown by amino acid sequencing to have a coding origin 3' to the env gene on the HTLV-III genome. The presence of antibodies to p27 in virus-exposed individuals indicated that this gene is functional in the natural host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Lee, T H -- McLane, M F -- Kanki, P J -- Groopman, J E -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA23885/CA/NCI NIH HHS/ -- CA37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):810-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997921" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acquired Immunodeficiency Syndrome/*immunology/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Viral/*immunology ; Antibody Formation ; Antigens, Viral/*immunology ; Deltaretrovirus/genetics/*immunology ; Electrophoresis, Polyacrylamide Gel ; Haplorhini/microbiology ; Humans ; Male ; Molecular Weight ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 1985-05-31
    Beschreibung: Antibodies from the serum of patients with the acquired immune deficiency syndrome (AIDS) or with the AIDS-related complex and from the serum of seropositive healthy homosexuals, recognize two major glycoproteins in cells infected with human T-cell lymphotropic virus type III (HTLV III). These glycoproteins, gp160 and gp120, are encoded by the 2.5-kilobase open reading frame located in the 3' end of the HTLV-III genome, as determined by amino terminus sequence analysis of the radiolabeled forms of these proteins. It is hypothesized that gp160 and gp120 represent the major species of virus-encoded envelope gene products for HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Barin, F -- McLane, M F -- Sodroski, J G -- Rosen, C A -- Haseltine, W A -- Lee, T H -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1091-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986290" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acquired Immunodeficiency Syndrome/*immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Viral/genetics/*immunology ; Base Sequence ; Deltaretrovirus/*immunology ; Genes, Viral ; Glycoproteins/genetics/immunology ; Humans ; Molecular Weight ; Tunicamycin/pharmacology ; Viral Envelope Proteins/genetics/*immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Publikationsdatum: 1985-11-15
    Beschreibung: The gene encoding the circumsporozoite (CS) protein of the human malaria parasite Plasmodium vivax has been cloned. The deduced sequence of the protein consists of 373 amino acids with a central region of 19 tandem repeats of the nonapeptide Asp-Arg-Ala-Asp/Ala-Gly-Gln-Pro-Ala-Gly. A synthetic 18-amino acid peptide containing two tandem repeats binds to a monoclonal antibody directed to the CS protein of Plasmodium vivax and inhibits the interaction of this antibody with the native protein in sporozoite extracts. The portions of the CS gene that do not contain repeats are closely related to the corresponding regions of the CS genes of two simian malarias, Plasmodium cynomolgi and Plasmodium knowlesi. In contrast, the homology between the CS genes of Plasmodium vivax and Plasmodium falciparum, another malaria parasite of humans, is very limited.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnot, D E -- Barnwell, J W -- Tam, J P -- Nussenzweig, V -- Nussenzweig, R S -- Enea, V -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):815-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414847" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Cloning, Molecular ; Epitopes/*genetics/immunology ; Haplorhini/parasitology ; Humans ; Malaria/parasitology ; Nucleic Acid Hybridization ; Plasmodium/immunology ; Plasmodium vivax/*genetics/immunology ; *Protozoan Proteins ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-07-05
    Beschreibung: Human T-lymphotropic virus type III (HTLV-III) encodes a trans-acting factor that activates the expression of genes linked to the HTLV-III long terminal repeat. By functional mapping of complementary DNA transcripts of viral messenger RNA's the major functional domain of the gene encoding this factor was localized to a region immediately before the env gene of the virus, a region previously thought to be noncoding. This newly identified gene consists of three exons, and its transcription into messenger RNA involves two splicing events bringing together sequences from the 5' part (287 base pairs), middle (268 base pairs), and 3'part (1258 base pairs) of the HTLV-III genome. A similar messenger RNA with a truncated second exon (70 base pairs) does not encode a trans-acting function. It is proposed that this second messenger RNA is the transcript of a gene (3'-orf) located after the env gene. Messenger RNA's were also identified for the env and gag-pol genes of HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Guo, C -- Josephs, S F -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):69-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990040" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Regulator ; *Genes, Viral ; Humans ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/genetics
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Publikationsdatum: 1985-05-24
    Beschreibung: In a study of recombinant proteins that might be useful in developing a vaccine against malaria, synthetic peptides from the circumsporozoite (CS) protein of Plasmodium falciparum were found to be immunogenic for mice and rabbits. Antibody to peptides from the repeating region of the CS protein recognized native CS protein and blocked sporozoite invasion of human hepatoma cells in vitro. Antibodies to peptides from regions I and II had no biologic activity, although antibody to region I recognized processed CS protein by Western blot analysis. These data support the feasibility of developing a vaccine against the sporozoite stage of the malaria parasite by using synthetic peptides of the repeating region of the CS protein conjugated to a carrier protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ballou, W R -- Rothbard, J -- Wirtz, R A -- Gordon, D M -- Williams, J S -- Gore, R W -- Schneider, I -- Hollingdale, M R -- Beaudoin, R L -- Maloy, W L -- New York, N.Y. -- Science. 1985 May 24;228(4702):996-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988126" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antibody Formation ; Antigens, Surface/*immunology ; Carcinoma, Hepatocellular ; Cell Line ; Cross Reactions ; Fluorescent Antibody Technique ; Humans ; Immune Sera/immunology ; Liver Neoplasms ; Malaria/prevention & control ; Mice ; Peptides/chemical synthesis/*immunology ; Plasmodium/immunology ; Plasmodium falciparum/*immunology/physiology ; Precipitin Tests ; *Protozoan Proteins ; Rabbits ; Vaccines/immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Publikationsdatum: 1985-12-06
    Beschreibung: Rat atrial natriuretic factor (ANF) is translated as a 152-amino acid precursor preproANF. PreproANF is converted to the 126-amino acid proANF, the storage form of ANF in the atria. ANF isolated from the blood is approximately 25 amino acids long. It is demonstrated here that rat cardiocytes in culture store and secrete proANF. Incubation of proANF with serum produced a smaller ANF peptide. PreproANF seems to be processed to proANF in the atria, and proANF appears to be released into the blood, where it is converted by a protease to a smaller peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bloch, K D -- Scott, J A -- Zisfein, J B -- Fallon, J T -- Margolies, M N -- Seidman, C E -- Matsueda, G R -- Homcy, C J -- Graham, R M -- Seidman, J G -- 1R23CA33570/CA/NCI NIH HHS/ -- HL07208/HL/NHLBI NIH HHS/ -- HL26215/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 6;230(4730):1168-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2933808" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Atrial Natriuretic Factor/*biosynthesis/genetics/secretion ; Autoradiography ; Cells, Cultured ; Electrophoresis, Polyacrylamide Gel ; Heart/physiology ; Immune Sera/immunology ; Myocardium/*cytology/metabolism ; Protein Precursors/*biosynthesis/genetics/secretion ; RNA, Messenger/genetics ; Rabbits/immunology ; Rats
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-06-07
    Beschreibung: Human DNA contains multiple copies of a novel class of endogenous retroviral genomes. Analysis of a human recombinant DNA clone (HLM-2) containing one such proviral genome revealed that it is a mosaic of retroviral-related sequences with the organization and length of known endogenous retroviral genomes. The HLM-2 long terminal repeat hybridized with the long terminal repeat of the squirrel monkey virus, a type D retrovirus. The HLM-2 gag and pol genes share extensive nucleotide sequence homology with those of the M432 retrovirus (a type A-related retrovirus), mouse mammary tumor virus (a type B retrovirus), and the avian Rous sarcoma virus (a type C retrovirus). Nucleotide sequence analysis revealed regions in the HLM-2 pol gene that were as much as 70 percent identical to the mouse mammary tumor virus pol gene. A portion of the putative HLM-2 env gene hybridized with the corresponding region of the M432 viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Callahan, R -- Chiu, I M -- Wong, J F -- Tronick, S R -- Roe, B A -- Aaronson, S A -- Schlom, J -- GM30400/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1208-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408338" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Antigens, Viral/genetics ; Base Sequence ; Cloning, Molecular ; DNA Restriction Enzymes ; Gene Products, gag ; Genes, Viral ; Humans ; RNA-Directed DNA Polymerase/genetics ; Retroviridae/classification/*genetics ; Viral Proteins/genetics
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 8
    Publikationsdatum: 1985-10-25
    Beschreibung: The retroviral transmembrane envelope protein p15E is immunosuppressive in that it inhibits immune responses of lymphocytes, monocytes, and macrophages. A region of p15E has been conserved among murine and feline retroviruses; a homologous region is also found in the transmembrane envelope proteins of the human retroviruses HTLV-I and HTLV-II and in a putative envelope protein encoded by an endogenous C-type human retroviral DNA. A peptide (CKS-17) was synthesized to correspond to this region of homology and was examined for its effects on lymphocyte proliferation. CKS-17 inhibited the proliferation of an interleukin-2-dependent murine cytotoxic T-cell line as well as alloantigen-stimulated proliferation of murine and human lymphocytes. Four other peptides, representing different regions of virus proteins, were inactive. These results suggest that the immunosuppressive portion of retroviral transmembrane envelope proteins may reside, at least in part, in a-conserved sequence represented by the CKS-17 peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cianciolo, G J -- Copeland, T D -- Oroszlan, S -- Snyderman, R -- P01-CA29589-02/CA/NCI NIH HHS/ -- R23-CA34671-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 25;230(4724):453-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996136" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Cell Line ; Deltaretrovirus/genetics ; Humans ; Leukemia Virus, Feline/genetics ; Leukemia Virus, Murine/genetics ; Lymphocyte Activation/*drug effects ; Lymphocyte Culture Test, Mixed ; Lymphocytes/drug effects ; Mice ; Mice, Inbred BALB C ; Peptides/*pharmacology ; Retroviridae/*genetics ; Spleen/cytology ; Viral Envelope Proteins/genetics/*pharmacology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 9
    Publikationsdatum: 1985-11-29
    Beschreibung: Amino acid sequence homology was found between viral and host encephalitogenic protein. Immune responses were then generated in rabbits by using the viral peptide that cross-reacts with the self protein. Mononuclear cell infiltration was observed in the central nervous systems of animals immunized with the viral peptide. Myelin basic protein (MBP) is a host protein whose encephalitogenic site of ten amino acids induces experimental allergic encephalomyelitis. By computer analysis, hepatitis B virus polymerase (HBVP) was found to share six consecutive amino acids with the encephalitogenic site of rabbit MBP. Rabbits given injections of a selected eight- or ten-amino acid peptide from HBVP made antibody that reacted with the predetermined sequences of HBVP and also with native MBP. Peripheral blood mononuclear cells from the immunized rabbits proliferated when incubated with either MBP or HBVP. Central nervous system tissue taken from these rabbits had a histologic picture reminiscent of experimental allergic encephalomyelitis. Thus, viral infection may trigger the production of antibodies and mononuclear cells that cross-react with self proteins by a mechanism termed molecular mimicry. Tissue injury from the resultant autoallergic event can take place in the absence of the infectious virus that initiated the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujinami, R S -- Oldstone, M B -- AG-04342/AG/NIA NIH HHS/ -- AI-07007/AI/NIAID NIH HHS/ -- NS-12428/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1043-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414848" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Autoimmune Diseases/immunology ; Cross Reactions ; *DNA-Directed RNA Polymerases/immunology ; Encephalomyelitis, Autoimmune, Experimental/immunology/*microbiology ; Hepatitis B virus/analysis/*immunology ; *Myelin Basic Protein/immunology ; *Viral Proteins/immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 10
    Publikationsdatum: 1985-08-23
    Beschreibung: The complete nucleotide sequence of the coding region of the circumsporozoite antigen gene (CS gene) of the Nuri strain of the malarial parasite Plasmodium knowlesi is presented. The gene from the Nuri strain exhibits a novel form of sequence diversity when compared to the CS gene from the H strain. Instead of the 12 tandem repeating 36-base pair units of the H strain, the Nuri strain contains 16 tandem repeating 27-base pair units of a different nucleotide sequence that encodes a different repeating peptide. In contrast, the 5' and 3' coding and noncoding sequences flanking the repeats are 98 percent conserved in both strains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Svec, P -- Mitchell, G H -- Godson, G N -- 1 R01 AI21496-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):779-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023712" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antigens, Protozoan/*genetics ; Antigens, Surface/genetics ; Base Sequence ; Genes ; Molecular Sequence Data ; Plasmodium/*genetics/immunology ; Protozoan Proteins/*genetics ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 11
    Publikationsdatum: 1985-12-20
    Beschreibung: Plasmodium vivax is one of the four malaria parasites that cause disease in humans. The structure of the immunodominant repeating peptide of the circumsporozoite (CS) protein of P. vivax was determined. A fragment of P. vivax DNA that encodes this tandemly repeating epitope was isolated by use of an oligonucleotide probe whose sequence is thought to be conserved in CS protein genes. DNA sequence analysis of the P. vivax clone indicates that the CS repeat is nine amino acids in length (Gly-Asp-Arg-Ala-Asp-Gly-Gln-Pro-Ala). The structure of the repeating region was confirmed with synthetic peptides and monoclonal antibodies directed against P. vivax sporozoites. This information should allow synthesis of a vaccine for P. vivax that is similar to the one being tested for P. falciparum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCutchan, T F -- Lal, A A -- de la Cruz, V F -- Miller, L H -- Maloy, W L -- Charoenvit, Y -- Beaudoin, R L -- Guerry, P -- Wistar, R Jr -- Hoffman, S L -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1381-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2416057" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Base Sequence ; DNA Restriction Enzymes ; Epitopes/*genetics ; *Genes ; Plasmodium vivax/*immunology ; Species Specificity
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 12
    Publikationsdatum: 1985-05-17
    Beschreibung: The amino acid sequences of the human low-density lipoprotein (LDL) receptor and the human precursor for epidermal growth factor (EGF) show 33 percent identity over a stretch of 400 residues. This region of homologous is encoded by eight contiguous exons in each respective gene. Of the nine introns that separate these exons, five are located in identical positions in the two protein sequences. This finding suggests that the homologous region may have resulted from a duplication of an ancestral gene and that the two genes evolved further by recruitment of exons from other genes, which provided the specific functional domains of the LDL receptor and the EGF precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Russell, D W -- Goldstein, J L -- Brown, M S -- Sanchez-Pescador, R -- Bell, G I -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):893-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3873704" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; *Base Sequence ; Biological Evolution ; Cloning, Molecular ; Epidermal Growth Factor/*genetics ; Genes ; Humans ; Protein Precursors/genetics ; Receptors, LDL/*genetics ; Repetitive Sequences, Nucleic Acid
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 13
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-05-17
    Beschreibung: The multifunctional nature of coated pit receptors predicts that these proteins will contain multiple domains. To establish the genetic basis for these domains (LDL) receptor. This gene is more than 45 kilobases in length and contains 18 exons, most of which correlate with functional domains previously defined at the protein level. Thirteen of the 18 exons encode protein sequences that are homologous to sequences in other proteins: five of these exons encode a sequence similar to one in the C9 component of complement; three exons encode a sequence similar to a repeat sequence in the precursor for epidermal growth factor (EGF) and in three proteins of the blood clotting system (factor IX, factor X, and protein C); and five other exons encode nonrepeated sequences that are shared only with the EGF precursor. The LDL receptor appears to be a mosaic protein built up of exons shared with different proteins, and it therefore belongs to several supergene families.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450672/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450672/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Goldstein, J L -- Brown, M S -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):815-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988123" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; *Base Sequence ; Cloning, Molecular ; Complement C9/genetics ; Dna ; Endonucleases ; Epidermal Growth Factor/genetics ; Factor IX/genetics ; Factor X/genetics ; *Genes ; Glycoproteins/genetics ; Humans ; Hyperlipoproteinemia Type II/genetics ; Molecular Weight ; Protein C ; Protein Precursors ; Protein Processing, Post-Translational ; Receptors, LDL/*genetics ; Repetitive Sequences, Nucleic Acid ; Single-Strand Specific DNA and RNA Endonucleases ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 14
    Publikationsdatum: 1985-06-28
    Beschreibung: The human T-cell leukemia viruses (HTLV) are replication-competent retroviruses whose genomes contain gag, pol, and env genes as well as a fourth gene, termed x, which is believed to be the transforming gene of HTLV. The product of the x gene is now shown to be encoded by a 2.1-kilobase messenger RNA derived by splicing of at least two introns. By means of S1 nuclease mapping of this RNA and nucleic acid sequence analysis of a complementary DNA clone, the complete primary structure of the x-gene product has been determined. It is encoded by sequences containing the env initiation codon and one nucleotide of the next codon spliced to the major open reading frame of the HTLV-I and HTLV-II x gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wachsman, W -- Golde, D W -- Temple, P A -- Orr, E C -- Clark, S C -- Chen, I S -- CA 30388/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1534-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990032" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Cell Transformation, Viral ; Codon ; Deltaretrovirus/*genetics ; Electrophoresis, Polyacrylamide Gel ; Humans ; Methionine/*genetics ; Rats ; Viral Proteins/*analysis
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 15
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-12-20
    Beschreibung: Electron microscopy of rotary-shadowed fibrinogen demonstrates that the molecules modified for crystallization by limited cleavage with a bacterial protease retain the major features of the native structure. This evidence, together with image processing and x-ray analysis of the crystals and of fibrin, has been used to develop a three-dimensional low resolution model for the molecule. The data indicate that the two large end domains of the molecule would be composed of the carboxyl-terminus of the B beta chain (proximal) and gamma chain (distal), respectively; the carboxyl-terminus of the A alpha chain would fold back to form an additional central domain. On this basis, the carboxyl-terminal region of each of the three chains of fibrinogen is folded independently into a globular domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weisel, J W -- Stauffacher, C V -- Bullitt, E -- Cohen, C -- AM17346/AM/NIADDK NIH HHS/ -- GM07596-07/GM/NIGMS NIH HHS/ -- HL30954/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1388-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071058" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Computers ; Fibrinogen/*metabolism ; Microscopy, Electron ; Models, Molecular ; Protein Conformation
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 16
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-05-10
    Beschreibung: The DNA coding for the human immunoglobulin D(IgD) heavy chain (delta, delta) has been sequenced including the membrane and secreted termini. Human delta, like that of the mouse, has a separate exon for the carboxyl terminus of the secreted form. This feature of human and mouse IgD distinguishes it from all other immunoglobulins regardless of species or class. The human gene is different from that of the mouse; it has three, rather than two, constant region domains; and its lengthy hinge is encoded by two exons rather than one. Except for the third constant region, the human and mouse genes are only distantly related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, M B -- Shen, A L -- Word, C J -- Tucker, P W -- Blattner, F R -- AI18016/AI/NIAID NIH HHS/ -- CA31013-04/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):733-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3922054" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Humans ; Immunoglobulin D/*genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin delta-Chains/*genetics ; Lymphocytes/metabolism ; Mice ; RNA, Messenger/genetics ; Species Specificity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 17
    Publikationsdatum: 1985-05-17
    Beschreibung: Clones of complementary DNA encoding the human lymphokine known as granulocyte-macrophage colony-stimulating factor (GM-CSF) were isolated by means of a mammalian cell (monkey COS cell) expression screening system. One of these clones was used to produce recombinant GM-CSF in mammalian cells. The recombinant hematopoietin was similar to the natural product that was purified to apparent homogeneity from medium conditioned by a human T-cell line. The human T-cell GM-CSF was found to be 60 percent homologous with the GM-CSF recently cloned from murine lung messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G G -- Witek, J S -- Temple, P A -- Wilkens, K M -- Leary, A C -- Luxenberg, D P -- Jones, S S -- Brown, E L -- Kay, R M -- Orr, E C -- New York, N.Y. -- Science. 1985 May 17;228(4701):810-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3923623" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Colony-Stimulating Factors/biosynthesis/*genetics/isolation & purification ; *Dna ; DNA, Recombinant ; *Granulocytes ; Haplorhini ; Humans ; *Macrophages ; RNA, Messenger/genetics ; T-Lymphocytes ; Transfection
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 18
    Publikationsdatum: 1985-04-19
    Beschreibung: Mammalian atria contain peptides that promote the excretion of salt and water from the kidney. When rat atrial tissue is extracted under conditions known to inhibit proteolysis, four natriuretic peptides, cardionatrins I to IV, are consistently isolated. These peptides derive from a common precursor, preprocardionatrin, of 152 amino acids, whose sequence was determined by DNA sequencing of a complementary DNA clone. Amino acid sequencing located the start points of cardionatrins I, III, and IV in the overall sequence. Cardionatrin IV most closely resembles procardionatrin because it begins immediately after the signal sequence at residue 25. Cardionatrin III begins at residue 73, and cardionatrin I, sequenced previously, begins at residue 123. Compositional analysis indicated that each of these cardionatrins extends up to tyrosine at position 150 but lacks the terminal two arginine residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, T G -- Davies, P L -- Kennedy, B P -- de Bold, M L -- de Bold, A J -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):323-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3157217" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Atrial Function ; Atrial Natriuretic Factor ; Base Sequence ; Chromatography, High Pressure Liquid ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Muscle Proteins/*genetics/isolation & purification ; *Peptide Fragments ; Protein Precursors/*genetics/isolation & purification ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 19
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-09-13
    Beschreibung: A psbA gene encoding the target of photosystem II herbicide inhibition, the 32,000-dalton thylakoid membrane protein, has been cloned from a mutant of Anacystis nidulans R2, which is resistant to 3-(3,4-dichlorophenyl)-1,1-dimethylurea-(diuron). A cloned DNA fragment from within the coding region of this gene transforms wild-type cells to herbicide resistance, proving that mutation within psbA is responsible for that phenotype. The mutation consists of a single nucleotide change that replaces serine at position 264 of the wild-type protein with alanine in that of the diuron-resistant mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golden, S S -- Haselkorn, R -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1104-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3929379" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Cyanobacteria/*genetics ; Diuron ; Drug Resistance ; Electrophoresis, Polyacrylamide Gel ; *Herbicides ; Membrane Proteins/genetics ; Molecular Weight ; *Mutation ; Phenotype
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 20
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-09-27
    Beschreibung: The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogle, J M -- Chow, M -- Filman, D J -- AI-20566/AI/NIAID NIH HHS/ -- AI-22346/AI/NIAID NIH HHS/ -- NS-07078/NS/NINDS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1358-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994218" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Antigens, Viral/immunology ; Capsid/physiology ; Chemical Phenomena ; Chemistry ; HeLa Cells/microbiology ; Mutation ; Poliovirus/physiology/*ultrastructure ; Protein Conformation ; Virus Replication ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 21
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-09-13
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jerne, N K -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1057-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035345" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antibodies/analysis ; Humans ; *Immune System ; Lymphocytes/physiology ; Mice
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 22
    Publikationsdatum: 1985-01-18
    Beschreibung: The T-cell receptor for antigen (Ti) was purified from the human tumor cell line HPB-ALL. Amino-terminal sequence analysis of an acid-cleaved peptide of the Ti alpha chain showed that it is highly homologous to a putative murine alpha chain recently described. Amino-terminal sequence analysis of the Ti beta chain revealed that it shares 50 percent homology with the Ti beta chain amino acid sequences from two other human T-cell tumors. Nucleotide sequence analysis of a complementary DNA clone encoding the Ti beta chain from the HPB-MLT cell line showed that this chain represents a second human constant region gene segment and suggested that it arises from direct joining of the variable and joining gene segments without any intervening D region sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, N -- Leiden, J -- Dialynas, D -- Fraser, J -- Clabby, M -- Kishimoto, T -- Strominger, J L -- Andrews, D -- Lane, W -- Woody, J -- 5 R01 AI15669/AI/NIAID NIH HHS/ -- AI10736/AI/NIAID NIH HHS/ -- Y001CP00502/CP/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 18;227(4684):311-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3871253" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Humans ; Immunoglobulin Constant Regions/genetics ; Leukemia, Lymphoid/immunology ; Lymphoma/immunology ; Mice ; Nucleic Acid Hybridization ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 23
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-10-04
    Beschreibung: A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified form of the Escherichia coli elongation factor Tu reveals that the GDP-binding domain has a structure similar to that of other nucleotide-binding proteins. The GDP ligand is located at the COOH-terminal end of the beta sheet and is linked to the protein via a Mg2+ ion salt bridge. The location of the guanine ring is unusual; the purine ring is located on the outer edge of the domain, not deep within a hydrophobic pocket. The amino acids from Pro10 to Arg44 and from Gly59 to Glu190 have been assigned to the electron density with computer graphic techniques, and the resulting model is consistent with all known biochemical data. An analysis of the structure reveals that four regions of the amino acid sequence that are homologous with the family of ras oncogene proteins, termed p21, are located in the vicinity of the GDP-binding site, and most of the invariant amino acids shared by the proteins interact directly with the GDP ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jurnak, F -- GM 26895/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):32-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898365" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Amino Acids/*analysis ; Binding Sites ; Chemistry, Physical ; Computers ; Escherichia coli ; Fourier Analysis ; Guanine Nucleotides/*analysis ; Guanosine Diphosphate/*analysis ; Magnesium/metabolism ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/*analysis ; Physicochemical Phenomena ; Protein Conformation ; Trypsin/metabolism ; X-Ray Diffraction
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 24
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-04-05
    Beschreibung: Induction of cytochrome P1-450 has been linked to susceptibility to certain chemically induced cancers in mouse and man. Treatment of the human cell line MCF-7 with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) results in high levels of aryl hydrocarbon (benzo[a]pyrene) hydroxylase (P1-450) activity. This cell line was used to isolate a human P1-450 full-length complementary DNA (cDNA) clone. The cDNA is 2566 nucleotides in length, encodes a polyadenylated messenger RNA (2.8 kilobases in length), and has a continuous reading frame producing a protein with 512 residues (molecular weight, 58,151). The human P1-450 cDNA and protein are 63 percent and 80 percent similar to mouse P1-450 cDNA and protein, respectively. Whereas the mouse TCDD-inducible P-450 gene subfamily has two members (P1-450 and P3-450), the human TCDD-inducible gene subfamily appears to have only one gene (P1-450).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaiswal, A K -- Gonzalez, F J -- Nebert, D W -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):80-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838385" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Carcinogens/pharmacology ; Cell Line ; Cricetinae ; Cytochrome P-450 Enzyme System/*genetics ; DNA/*genetics ; Dioxins/*pharmacology ; Enzyme Induction ; Humans ; Mice ; Nucleic Acid Hybridization ; Rabbits ; Tetrachlorodibenzodioxin/*pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 25
    Publikationsdatum: 1985-10-18
    Beschreibung: Complementary DNA (cDNA) clones encoding human macrophage-specific specific colony-stimulating factor (CSF-1) were isolated. One cDNA clone codes for a mature polypeptide of 224 amino acids and a putative leader of 32 amino acids. This cDNA, which was cloned in the Okayama-Berg expression vector, specifies the synthesis of biologically active CSF-1 in COS cells, as determined by a specific radioreceptor assay, macrophage bone marrow colony formation, and antibody neutralization. Most of the cDNA isolates contain part of an intron sequence that changes the reading frame, resulting in an abrupt termination of translation; these cDNA's were inactive in COS cells. The CSF-1 appears to be encoded by a single-copy gene, but its expression results in the synthesis of several messenger RNA species, ranging in size from about 1.5 to 4.5 kilobases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawasaki, E S -- Ladner, M B -- Wang, A M -- Van Arsdell, J -- Warren, M K -- Coyne, M Y -- Schweickart, V L -- Lee, M T -- Wilson, K J -- Boosman, A -- C32551/PHS HHS/ -- New York, N.Y. -- Science. 1985 Oct 18;230(4723):291-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996129" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Colony-Stimulating Factors/*genetics ; DNA/*metabolism ; DNA Restriction Enzymes ; *Genes ; Humans ; Macrophages/*metabolism ; Pancreatic Neoplasms ; RNA, Messenger/genetics ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 26
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-09-06
    Beschreibung: The cellular gene encoding the receptor for epidermal growth factor (EGF) has considerable homology to the oncogene of avian erythroblastosis virus. In a human mammary carcinoma, a DNA sequence was identified that is related to v-erbB but amplified in a manner that appeared to distinguish it from the gene for the EGF receptor. Molecular cloning of this DNA segment and nucleotide sequence analysis revealed the presence of two putative exons in a DNA segment whose predicted amino acid sequence was closely related to, but different from, the corresponding sequence of the erbB/EGF receptor. Moreover, this DNA segment identified a 5-kilobase transcript distinct from the transcripts of the EGF receptor gene. Thus, a new member of the tyrosine kinase proto-oncogene family has been identified on the basis of its amplification in a human mammary carcinoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Kraus, M H -- Aaronson, S A -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):974-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992089" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Breast Neoplasms/*genetics ; Cell Line ; Cloning, Molecular ; DNA, Neoplasm/*genetics ; Female ; *Gene Amplification ; Gene Expression Regulation ; Humans ; *Oncogenes ; Protein Kinases/*genetics ; Protein-Tyrosine Kinases ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/*genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 27
    Publikationsdatum: 1985-10-04
    Beschreibung: Apolipoprotein (apo-) B is the ligand responsible for the receptor-mediated catabolism of low density lipoproteins, the principal cholesterol-transporting lipoproteins in plasma. The primary structure of the carboxyl-terminal 30 percent (1455 amino acids) of human apo-B (apo-B100) has been deduced from the nucleotide sequence of complementary DNA. Portions of the protein structure that may relate to its receptor binding function and lipid binding properties have been identified. The apo-B100 messenger RNA is about 19 kilobases in length. The apo-B100 gene is expressed primarily in liver and, to a lesser extent, in small intestine, but in no other tissues. The gene for apo-B100 is located in the p24 region (near the tip of the short arm) of chromosome 2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knott, T J -- Rall, S C Jr -- Innerarity, T L -- Jacobson, S F -- Urdea, M S -- Levy-Wilson, B -- Powell, L M -- Pease, R J -- Eddy, R -- Nakai, H -- GM 20454/GM/NIGMS NIH HHS/ -- HO 05196/HO/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):37-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994225" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Apolipoprotein B-100 ; Apolipoproteins B/analysis/*genetics ; Apolipoproteins E/analysis ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Human, 1-3 ; DNA/analysis ; DNA Restriction Enzymes/metabolism ; Female ; *Gene Expression Regulation ; Haplorhini ; Humans ; Intestine, Small/metabolism ; Lipid Metabolism ; Lipoproteins, LDL/metabolism ; Liver/metabolism ; Mice ; RNA, Messenger/analysis ; Receptors, LDL/metabolism ; Structure-Activity Relationship
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 28
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-06-28
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1517-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012306" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Biological Transport ; Enzyme Precursors/metabolism ; Mitochondria/*metabolism ; Mitochondria, Liver/enzymology ; Ornithine Carbamoyltransferase/metabolism ; Peptides/*metabolism ; Protein Sorting Signals ; Proteins/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 29
    Publikationsdatum: 1985-06-07
    Beschreibung: The 55 codons upstream of the gene sequence encoding the hepatitis B surface antigen (HBsAg) are called the pre-S(2) region. It has been proposed that polypeptides of high molecular weight that contain the pre-S(2) region should be included in future hepatitis B virus (HBV) vaccines. The pre-S(2) region and the S gene product [25 kilodalton (kD)] together compose a polypeptide of high molecular weight (33 kD). As an initial attempt to determine the relevance of the 33-kD polypeptide to development of an HBV vaccine, the murine immune response to pre-S(2)-encoded determinants as compared to S-encoded determinants on the same polypeptide was examined. The results indicate (i) the pre-S(2) region is significantly more immunogenic than the S region of HBsAg, (ii) the 26 amino acid residues at the NH2-terminus of the 33-kD polypeptide represent a dominant antibody binding site on the pre-S(2) region, (iii) the immune response to the pre-S(2) region is regulated by H-2-linked genes distinct from those that regulate the response to the S region, and (iv) immunization of an S region nonresponder strain with HBV envelope particles that contain both the pre-S(2) and S regions can circumvent nonresponsiveness to the S region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milich, D R -- Thornton, G B -- Neurath, A R -- Kent, S B -- Michel, M L -- Tiollais, P -- Chisari, F V -- AI 00585/AI/NIAID NIH HHS/ -- AI 20001/AI/NIAID NIH HHS/ -- AI 20720/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1195-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408336" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antibody Formation ; Antibody Specificity ; Epitopes ; Genes, MHC Class II ; Genes, Viral ; Hepatitis B Antibodies/immunology ; Hepatitis B Surface Antigens/genetics/*immunology ; Mice ; Molecular Weight ; Protein Precursors/genetics/immunology ; Viral Hepatitis Vaccines/*immunology ; Viral Proteins/genetics/immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 30
    Publikationsdatum: 1985-04-05
    Beschreibung: A bovine retinal complementary DNA clone encoding the alpha subunit of transducin (T alpha) was isolated with the use of synthetic oligodeoxynucleotides as probes, and the complete nucleotide sequence of the insert was determined. THe predicted protein sequence of 354 amino acids includes the known sequences of four tryptic peptides and sequences adjacent to the residues that undergo adenosine diphosphate ribosylation by cholera toxin and pertussis toxin. On the basis of homologies to other proteins, such as the elongation factors of protein synthesis and the ras oncogene proteins, regions are identified that are predicted to be acylated and involved in guanine nucleotide binding and hydrolysis. Amino acid sequence similarity between T alpha and ras is confined to these regions of the molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lochrie, M A -- Hurley, J B -- Simon, M I -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):96-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856323" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Bacterial Toxins/metabolism ; Base Sequence ; Cattle ; Cholera Toxin/metabolism ; Cloning, Molecular ; DNA/genetics ; Guanosine Triphosphate/metabolism ; Membrane Proteins/*genetics/metabolism ; *Oncogenes ; Peptide Elongation Factors/*genetics ; Pertussis Toxin ; Transducin ; Virulence Factors, Bordetella
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 31
    Publikationsdatum: 1985-02-01
    Beschreibung: The nucleotide sequence of molecular clones of DNA from a retrovirus, ARV-2, associated with the acquired immune deficiency syndrome (AIDS) was determined. Proviral DNA of ARV-2 (9737 base pairs) has long terminal repeat structures (636 base pairs) and long open reading frames encoding gag (506 codons), pol (1003 codons), and env (863 codons) genes. Two additional open reading frames were identified. Significant amino acid homology with several other retroviruses was noted in the predicted product of gag and pol, but ARV-2 was as closely related to murine and avian retroviruses as it was to human T-cell leukemia viruses (HTLV-I and HTLV-II). By means of an SV-40 vector in transfected simian cells, the cloned gag and env genes of ARV-2 were shown to express viral proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez-Pescador, R -- Power, M D -- Barr, P J -- Steimer, K S -- Stempien, M M -- Brown-Shimer, S L -- Gee, W W -- Renard, A -- Randolph, A -- Levy, J A -- New York, N.Y. -- Science. 1985 Feb 1;227(4686):484-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2578227" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acquired Immunodeficiency Syndrome/*microbiology ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon ; DNA, Viral/*genetics ; Deltaretrovirus/genetics ; Gene Products, gag ; Genes, Viral ; Humans ; Nucleic Acid Conformation ; RNA-Directed DNA Polymerase/biosynthesis/genetics ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*genetics ; Viral Envelope Proteins/biosynthesis/genetics ; Viral Proteins/biosynthesis/*genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 32
    Publikationsdatum: 1985-04-12
    Beschreibung: Tumor necrosis factor (TNF) is a soluble protein that causes damage to tumor cells but has no effect on normal cells. Human TNF was purified to apparent homogeneity as a 17.3-kilodalton protein from HL-60 leukemia cells and showed cytotoxic and cytostatic activities against various human tumor cell lines. The amino acid sequence was determined for the amino terminal end of the purified protein, and oligodeoxyribonucleotide probes were synthesized on the basis of this sequence. Complementary DNA (cDNA) encoding human TNF was cloned from induced HL-60 messenger RNA and was confirmed by hybrid-selection assay, direct expression in COS-7 cells, and nucleotide sequence analysis. The human TNF cDNA is 1585 base pairs in length and encodes a protein of 233 amino acids. The mature protein begins at residue 77, leaving a long leader sequence of 76 amino acids. Expression of high levels of human TNF in Escherichia coli was accomplished under control of the bacteriophage lambda PL promoter and gene N ribosome binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A M -- Creasey, A A -- Ladner, M B -- Lin, L S -- Strickler, J -- Van Arsdell, J N -- Yamamoto, R -- Mark, D F -- New York, N.Y. -- Science. 1985 Apr 12;228(4696):149-54.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3856324" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cells, Cultured ; *Cloning, Molecular ; DNA/*genetics ; DNA, Recombinant/metabolism ; Glycoproteins/*genetics/isolation & purification/pharmacology ; Humans ; Leukemia, Myeloid/metabolism ; Mice ; Mice, Nude ; Neoplasms, Experimental/drug therapy ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Rabbits ; Rats ; Tumor Necrosis Factor-alpha ; Xenopus
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 33
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-11-15
    Beschreibung: Systematic studies on the significance of the secretory-like morphological characteristic of cardiac atrial muscle cells of mammals led to the finding that these cells produce a polypeptide hormone. This hormone, described in 1981 as atrial natriuretic factor (ANF), is diuretic (natriuretic), hypotensive, and has an inhibitory effect on renin and aldosterone secretion. Thus, ANF probably intervenes in the short- and long-term control of water and electrolyte balance and of blood pressure. Phylogenetically, ANF appears early, suggesting different functions for this peptide in accordance with each species' environment. Knowledge of the properties of the hormone should provide insights into the pathophysiology of important clinical entities and lead to the development of new pharmaceutical products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Bold, A J -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):767-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2932797" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Amphibians ; Animals ; Atrial Function ; Atrial Natriuretic Factor/genetics/*physiology ; Birds ; Cattle ; Cytoplasmic Granules/ultrastructure ; Fishes ; Heart/*physiology ; Humans ; Microscopy, Electron ; Myocardium/cytology/ultrastructure ; Rats ; Reptiles ; Rodentia ; Sinoatrial Node/cytology/physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 34
    Publikationsdatum: 1985-06-07
    Beschreibung: The concentration in plasma of the female protein (FP) of the golden Syrian hamster is regulated by sex steroids and by mediators of the acute-phase response to tissue injury or inflammation. A complementary DNA (cDNA) clone corresponding to FP was isolated from a hamster liver cDNA library and used to determine the nucleotide sequence and derived amino acid sequence of native FP. The primary sequence of FP is 69 percent identical to human serum amyloid P component and 50 percent identical to human C-reactive protein. Evidence showed that sex-limited and acute-phase control of the FP gene is pretranslational. The FP protein is thus a useful model for investigating dual regulation of expression of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dowton, S B -- Woods, D E -- Mantzouranis, E C -- Colten, H R -- AI20959/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408337" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acute-Phase Proteins ; Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Blood Proteins/genetics ; *C-Reactive Protein ; Cricetinae/*physiology ; DNA/genetics ; Female ; Gene Expression Regulation ; Genes ; Liver/physiology ; Male ; Mesocricetus/*physiology ; RNA, Messenger/genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 35
    Publikationsdatum: 1985-04-19
    Beschreibung: A general method for modifying eukaryotic genes by site-specific mutagenesis and subsequent expression in mammalian cells was developed to study the relation between structure and function of the proteolytic enzyme trypsin. Glycine residues at positions 216 and 226 in the binding cavity of trypsin were replaced by alanine residues, resulting in three trypsin mutants. Computer graphic analysis suggested that these substitutions would differentially affect arginine and lysine substrate binding of the enzyme. Although the mutant enzymes were reduced in catalytic rate, they showed enhanced substrate specificity relative to the native enzyme. This increased specificity was achieved by the unexpected differential effects on the catalytic activity toward arginine and lysine substrates. Mutants containing alanine at position 226 exhibited an altered conformation that may be converted to a trypsin-like structure upon binding of a substrate analog.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Largman, C -- Fletcher, T -- Roczniak, S -- Barr, P J -- Fletterick, R -- Rutter, W J -- AM26081/AM/NIADDK NIH HHS/ -- GM07216/GM/NIGMS NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):291-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838593" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; DNA/genetics ; Electrophoresis ; Mutation ; Rats ; Substrate Specificity ; Trypsin/biosynthesis/*genetics/metabolism ; Trypsinogen/metabolism
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    Standort Signatur Erwartet Verfügbarkeit
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  • 36
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-05-31
    Beschreibung: The complement cleavage product C5a is a potent stimulant of inflammatory processes; thus, inhibition of C5a activity is of therapeutic interest. The three-dimensional structure of the major portion of C5a was modeled from the homologous C3a crystal structure by comparative modeling techniques. The model shows that core residues of C5a are completely conserved, while external residues differ from C3a. Even though the amino-terminal 12 residues of C3a are disordered in the crystal, this sequence in C5a may form an amphipathic helix. The distribution of species sequence differences in the complete C5a structure suggests a possible receptor binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greer, J -- New York, N.Y. -- Science. 1985 May 31;228(4703):1055-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3992245" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; *Complement C5/metabolism ; Complement C5a ; Crystallography ; Humans ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Receptors, Complement/metabolism ; Thermodynamics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 37
    Publikationsdatum: 1985-09-20
    Beschreibung: A complementary DNA clone encoding the alpha subunit of the adenylate cyclase stimulatory G protein (Gs) was isolated and identified. A bovine brain complementary DNA library was screened with an oligonucleotide probe derived from amino acid sequence common to known G proteins. The only clone that was obtained with this probe has a complementary DNA insert of approximately 1670 base pairs. An antibody to a peptide synthesized according to deduced amino acid sequence reacts specifically with the alpha subunit of Gs. In addition, RNA that hybridizes with probes made from the clone is detected in wild-type S49 cells; however, cyc- S49 cells, which are deficient in Gs alpha activity, are devoid of this messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harris, B A -- Robishaw, J D -- Mumby, S M -- Gilman, A G -- GM09731/GM/NIGMS NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1274-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839937" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenylyl Cyclases/*metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Cerebral Cortex ; *Cloning, Molecular ; DNA/*analysis ; Enzyme Activation ; Nerve Tissue Proteins/*genetics ; Nucleic Acid Hybridization ; Protein Biosynthesis ; Retina
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 38
    Publikationsdatum: 1985-11-08
    Beschreibung: The gene encoding the human interleukin-2 (IL-2) receptor consists of 8 exons spanning more than 25 kilobases on chromosome 10. Exons 2 and 4 were derived from a gene duplication event and unexpectedly also are homologous to the recognition domain of human complement factor B. Alternative messenger RNA (mRNA) splicing may delete exon 4 sequences, resulting in a mRNA that does not encode a functional IL-2 receptor. Leukemic T cells infected with HTLV-I and normal activated T cells express IL-2 receptors with identical deduced protein sequences. Receptor gene transcription is initiated at two principal sites in normal activated T cells. Adult T cell leukemia cells infected with HTLV-I show activity at both of these sites, but also at a third transcription initiation site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leonard, W J -- Depper, J M -- Kanehisa, M -- Kronke, M -- Peffer, N J -- Svetlik, P B -- Sullivan, M -- Greene, W C -- New York, N.Y. -- Science. 1985 Nov 8;230(4726):633-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996141" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Complement Factor B/genetics ; DNA/genetics/isolation & purification ; DNA, Recombinant/isolation & purification ; Deltaretrovirus ; *Genes, MHC Class II ; Humans ; Peptide Chain Initiation, Translational ; RNA, Messenger/genetics ; Receptors, Immunologic/biosynthesis/*genetics ; Receptors, Interleukin-2 ; Repetitive Sequences, Nucleic Acid ; Retroviridae Infections/genetics ; T-Lymphocytes/microbiology ; Transcription, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 39
    Publikationsdatum: 1985-12-20
    Beschreibung: To paralyze their more agile prey, the venomous fish-hunting cone snails (Conus) have developed a potent biochemical strategy. They produce several classes of toxic peptides (conotoxins) that attack a series of successive physiological targets in the neuromuscular system of the fish. The peptides include presynaptic omega-conotoxins that prevent the voltage-activated entry of calcium into the nerve terminal and release of acetylcholine, postsynaptic alpha-conotoxins that inhibit the acetylcholine receptor, and muscle sodium channel inhibitors, the mu-conotoxins, which directly abolish muscle action potentials. These distinct peptide toxins share several common features: they are relatively small (13 to 29 amino acids), are highly cross-linked by disulfide bonds, and strongly basic. The fact that they inhibit sequential steps in neuromuscular transmission suggests that their action is synergistic rather than additive. Five new omega-conotoxins that block presynaptic calcium channels are described. They vary in their activity against different vertebrate classes, and also in their actions against different synapses from the same animal. There are susceptible forms of the target molecule in peripheral synapses of fish and amphibians, but those of mice are resistant. However, the mammalian central nervous system is clearly affected, and these toxins are thus of potential significance for investigating the presynaptic calcium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olivera, B M -- Gray, W R -- Zeikus, R -- McIntosh, J M -- Varga, J -- Rivier, J -- de Santos, V -- Cruz, L J -- GM 22737/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1338-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071055" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Feeding Behavior ; Fishes ; Mice ; Mollusk Venoms/*isolation & purification/toxicity ; Neurotoxins/*isolation & purification ; Peptide Fragments/analysis ; Snails/*physiology ; Species Specificity ; Structure-Activity Relationship
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 40
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-04-19
    Beschreibung: The milk protein beta-lactoglobulin has been extensively studied but its function has not been identified. A clue regarding the function of a protein can be obtained by discovering a genetic relationship with a protein of known function through comparisons of amino acid sequence. Such comparisons revealed that beta-lactoglobulin is similar to human serum retinol-binding protein and to another human protein of unknown function known as complex-forming glycoprotein heterogeneous in charge (protein HC). beta-Lactoglobulins from several species have been found to bind retinol, while the absorption and fluorescence properties reported for the unidentified heterogeneous prosthetic group of protein HC are retinoid-like. The role of serum retinol-binding protein in vitamin A transport in the circulation suggests that the other two homologous proteins may function in the binding and transport of retinoids; beta-lactoglobulin may facilitate the absorption of vitamin A from milk and protein HC may mediate the excretion of retinol-derived metabolites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pervaiz, S -- Brew, K -- GM 21363/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):335-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580349" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alpha-Globulins/*genetics ; Amino Acid Sequence ; Animals ; Cattle ; Dolphins ; Humans ; Lactoglobulins/*genetics/metabolism ; Lagomorpha ; Mammals ; Milk/metabolism ; Primates ; Protein Conformation ; Proteinuria/metabolism ; Retinol-Binding Proteins/*genetics/metabolism ; Rodentia ; Swine ; Vitamin A/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 41
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-10-11
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1985 Oct 11;230(4722):161.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4035360" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Angiogenesis Inducing Agents/genetics/*isolation & purification ; Animals ; Growth Substances/*isolation & purification ; Humans ; Neoplasm Proteins/genetics/*isolation & purification ; Neoplasms/blood supply/metabolism ; Rats ; *Ribonuclease, Pancreatic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 42
    Publikationsdatum: 1985-11-29
    Beschreibung: Cell surface molecules of eukaryotic cells have been considered to be integrated into the membrane bilayer by a transmembrane protein sequence. The Thy-1 antigen of rodent thymocytes and brain was the first eukaryotic membrane molecule for which biochemical data clearly suggested membrane integration via a nonprotein tail. Direct evidence is now presented showing that a glycophospholipid structure is attached to the carboxyl-terminal cysteine residue and that 31 carboxyl-terminal amino acids predicted from the Thy-1 complementary DNA sequence are not present in the mature glycoprotein. These experimental results raise questions concerning signaling across a cell membrane since antibodies to Thy-1 can stimulate T lymphocytes to release lymphokines and undergo cell division.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tse, A G -- Barclay, A N -- Watts, A -- Williams, A F -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1003-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2865810" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; *Antigens, Surface/isolation & purification ; Antigens, Thy-1 ; Brain/*metabolism ; Ethanolamines/metabolism ; Galactosamine/metabolism ; Glucosamine/metabolism ; Glycolipids/*metabolism ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Rats ; Stearic Acids/metabolism ; T-Lymphocytes/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 43
    Publikationsdatum: 1985-09-13
    Beschreibung: Mutations have been identified in variants of poliovirus, type 1 (Mahoney) on the basis of their resistance to neutralization by individual monoclonal antibodies. The phenotypes of these variants were defined in terms of antibody binding; the pattern of epitopes expressed or able to be exploited for neutralization were complex. Single amino acid changes can have distant (in terms of linear sequence) and generalized effects on the antigenic structure of poliovirus and similarly constituted virions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, D C -- Jameson, B A -- Bonin, J -- Kohara, M -- Abe, S -- Itoh, H -- Komatsu, T -- Arita, M -- Kuge, S -- Nomoto, A -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1090-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2412292" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Amino Acids/analysis ; Antibodies, Monoclonal ; Epitopes/*analysis ; Immunity, Innate ; Mutation ; Phenotype ; Poliovirus/genetics/*immunology ; Virion/immunology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 44
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-11-01
    Beschreibung: The major light-harvesting complex in cyanobacteria and red algae, the phycobilisome, is composed of chromophoric and nonchromophoric polypeptides. Two linked genes encoding major chromophoric components, the polypeptide subunits of phycocyanin, were isolated from the cyanobacterium Fremyella diplosiphon. Transcripts from this phycocyanin subunit gene cluster were present as major species in the cyanobacterium grown in red light, but not in cultures maintained in green light. The genes for the subunits of the red light-induced phycocyanin were transcribed together (beta-phycocyanin followed by alpha-phycocyanin) on two messenger RNA species; one contained 1600 bases while the other had 3800 bases. The latter, which encompassed the smaller transcript, contained additional sequences extending from the 3' end of the coding region of the alpha-phycocyanin gene. It may encode other light-induced components of the phycobilisome. Since phycocyanin, which effectively absorbs red light, becomes a dominant constituent of the phycobilisome in red light, these different levels may reflect an important adaptive mechanism of these organisms to their environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conley, P B -- Lemaux, P G -- Grossman, A R -- GM 33436-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):550-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3931221" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Cyanobacteria/*genetics ; Light ; Nucleic Acid Hybridization ; Phycobilisomes ; Phycocyanin/genetics ; RNA, Messenger/metabolism ; *Transcription, Genetic
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 45
    Publikationsdatum: 1985-12-20
    Beschreibung: Bovine brain-derived acidic fibroblast growth factor (aFGF) is a protein mitogen originally identified in partially purified preparations of whole brain. The protein was purified to homogeneity and shown to be a potent vascular endothelial cell mitogen in culture and angiogenic substance in vivo. The homology of aFGF to human interleukin-1 beta was inferred from partial sequence data. The complete amino acid sequence of aFGF has now been determined and observed to be similar to both basic FGF and interleukin-1's. A neuropeptide-like sequence, flanked by basic dipeptides, was observed within the aFGF sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gimenez-Gallego, G -- Rodkey, J -- Bennett, C -- Rios-Candelore, M -- DiSalvo, J -- Thomas, K -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1385-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071057" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; *Brain Chemistry ; Cattle ; Fibroblast Growth Factors/*isolation & purification ; Hormones ; Humans ; Hydrogen-Ion Concentration ; Nerve Tissue Proteins ; Sequence Homology, Nucleic Acid ; Species Specificity
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 46
    Publikationsdatum: 1985-09-06
    Beschreibung: The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueckler, M -- Caruso, C -- Baldwin, S A -- Panico, M -- Blench, I -- Morris, H R -- Allard, W J -- Lienhard, G E -- Lodish, H F -- GM22996/GM/NIGMS NIH HHS/ -- HL32262/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):941-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839598" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; *Carrier Proteins/genetics/metabolism ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/genetics ; Erythrocytes/metabolism ; Glucose/*metabolism ; Humans ; Liver Neoplasms, Experimental/metabolism ; *Membrane Proteins/genetics/metabolism ; Molecular Weight ; Monosaccharide Transport Proteins ; Protein Conformation ; RNA, Messenger/genetics ; Tissue Distribution
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 47
    Publikationsdatum: 1985-08-09
    Beschreibung: Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linzen, B -- Soeter, N M -- Riggs, A F -- Schneider, H J -- Schartau, W -- Moore, M D -- Yokota, E -- Behrens, P Q -- Nakashima, H -- Takagi, T -- GM 21314/GM/NIGMS NIH HHS/ -- GM 28410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):519-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023698" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Arachnida/genetics ; *Arthropods/genetics ; Binding Sites ; Biological Evolution ; Chemical Phenomena ; Chemistry ; Copper ; Crustacea/genetics ; *Hemocyanin/genetics ; Models, Molecular ; Protein Conformation ; Species Specificity
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 48
    Publikationsdatum: 1985-01-25
    Beschreibung: The transforming protein of Rous sarcoma virus, p60src, was shown to be acylated at its amino terminus with the long-chain fatty acid myristic acid by isolation of a tryptic peptide with the following structure: myristylglycylserylseryllysine. The occurrence of this unusual posttranslational modification in the cyclic adenosine monophosphate-dependent protein kinase and in several transforming protein kinases of mammalian retroviruses suggests that myristylation of the amino terminal glycyl residue may be critical for the function of certain proteins related to cell transformation and growth control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, A M -- Henderson, L E -- Oroszlan, S -- Garber, E A -- Hanafusa, H -- CA-14935/CA/NCI NIH HHS/ -- N01-CO-23909/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):427-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3917576" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acylation ; Amino Acid Sequence ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; Myristic Acid ; Myristic Acids/*analysis/metabolism ; Oncogene Protein pp60(v-src) ; Protein Kinases/*analysis/metabolism ; Protein Processing, Post-Translational ; Viral Proteins/*analysis/metabolism
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 49
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1985-02-08
    Beschreibung: The mode of integration of the glycoprotein thy-1 within the cell membrane has been controversial due to an apparent lack of a transmembrane hydrophobic segment. Rat and mouse complementary DNA and genomic clones encoding the thy-1 molecule have been isolated and sequenced. These studies have enabled us to determine the intron-exon organization of the thy-1 gene. Furthermore, they have revealed the existence of a sequence which would encode an extra segment (31 amino acids) at the carboxyl terminus of the thy-1 molecule. These extra amino acids include a 20-amino acid hydrophobic segment which may be responsible for integration of thy-1 within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seki, T -- Chang, H C -- Moriuchi, T -- Denome, R -- Ploegh, H -- Silver, J -- CA38404/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 8;227(4687):649-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857501" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Antigens, Thy-1 ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Weight ; Nucleic Acid Hybridization ; Rats
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 50
    Publikationsdatum: 1985-09-27
    Beschreibung: Radiolabeled amino acid sequencing was used to characterize gp41, an antigen of HTLV-III/LAV, the virus believed to be the etiological agent of the acquired immune deficiency syndrome. This antigen is the one most commonly detected in immunoblot assays by sera of patients with AIDS or AIDS-related complex (ARC) and other individuals infected with HTLV-III/LAV. A mouse monoclonal antibody that was reactive with gp41 precipitated a 160-kilodalton protein (gp160) in addition to gp41, but did not precipitate a 120-kilodalton protein (gp120) from extracts of metabolically labeled cells producing HTLV-III. Extracts of infected cells that had been labeled with tritiated leucine or isoleucine were immunoprecipitated with the monoclonal antibody. The immunoprecipitates were fractionated by polyacrylamide gel electrophoresis and the p41 was eluted from the gel bands and subjected to amino-terminal radiolabeled amino acid sequencing by the semiautomated Edman degradation. Leucine residues occurred in cycles 7, 9, 12, 26, 33, and 34 among 40 cycles and isoleucine occurred in cycle 4 among 24 cycles analyzed. Comparison of the data with the deduced amino acid sequence of the env gene product of HTLV-III precisely placed gp41 in the COOH-terminal region of the env gene product. Gp160 is thus the primary env gene product and it is processed into gp120 and gp41.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veronese, F D -- DeVico, A L -- Copeland, T D -- Oroszlan, S -- Gallo, R C -- Sarngadharan, M G -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1402-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994223" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Viral/genetics/immunology ; Deltaretrovirus/*genetics ; *Genes, Viral ; Humans ; Mice ; Mice, Inbred BALB C ; Viral Envelope Proteins/*genetics
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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